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Glucosyl-3-phosphoglycerate synthase (GpgS) (EC 2.4.1.266)

 GPGS_PETMO              Reviewed;         325 AA.
A9BHI9;
07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 1.
18-JUL-2018, entry version 60.
RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000303|PubMed:20061481};
Short=GpgS {ECO:0000305};
EC=2.4.1.266 {ECO:0000269|PubMed:20061481};
Name=gpgS {ECO:0000303|PubMed:20061481};
OrderedLocusNames=Pmob_1142 {ECO:0000312|EMBL:ABX31861.1};
Petrotoga mobilis (strain DSM 10674 / SJ95).
Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
NCBI_TaxID=403833;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 10674 / SJ95;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D.,
Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
Hauser L., Kyrpides N., Mikhailova N., Noll K., Richardson P.;
"Complete sequence of Petroga mobilis SJ95.";
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
STRAIN=DSM 10674 / SJ95;
PubMed=20061481; DOI=10.1128/JB.01424-09;
Fernandes C., Mendes V., Costa J., Empadinhas N., Jorge C., Lamosa P.,
Santos H., da Costa M.S.;
"Two alternative pathways for the synthesis of the rare compatible
solute mannosylglucosylglycerate in Petrotoga mobilis.";
J. Bacteriol. 192:1624-1633(2010).
-!- FUNCTION: Involved in the biosynthesis of the compatible solute
mannosylglucosylglycerate through a phosphorylating pathway.
Catalyzes the transfer of a glucose (Glc) moiety from uridine
diphosphate (UDP-Glc) to the position 2 of 3-phospho-D-glycerate
(3-PGA) to form glucosyl-3-phosphoglycerate (GPG). UDP-glucose is
the preferred substrate, but it can be partially replaced by ADP-
glucose. {ECO:0000269|PubMed:20061481}.
-!- CATALYTIC ACTIVITY: NDP-glucose + 3-phospho-D-glycerate = NDP + 2-
O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate.
{ECO:0000269|PubMed:20061481}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:20061481};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20061481};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:20061481};
Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
Evidence={ECO:0000269|PubMed:20061481};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:20061481};
Note=Requires divalent cations for activity.
{ECO:0000269|PubMed:20061481};
-!- ENZYME REGULATION: Inhibited by ADP and EDTA.
{ECO:0000269|PubMed:20061481}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.7 mM for 3-PGA (at 60 degrees Celsius)
{ECO:0000269|PubMed:20061481};
KM=0.5 mM for 3-PGA (at 70 degrees Celsius)
{ECO:0000269|PubMed:20061481};
KM=1.0 mM for UDP-glucose (at 60 degrees Celsius)
{ECO:0000269|PubMed:20061481};
KM=0.9 mM for UDP-glucose (at 70 degrees Celsius)
{ECO:0000269|PubMed:20061481};
Vmax=43.9 umol/min/mg enzyme toward 3-PGA (at 60 degrees
Celsius) {ECO:0000269|PubMed:20061481};
Vmax=65.0 umol/min/mg enzyme toward 3-PGA (at 70 degrees
Celsius) {ECO:0000269|PubMed:20061481};
Vmax=44.0 umol/min/mg enzyme toward UDP-glucose (at 60 degrees
Celsius) {ECO:0000269|PubMed:20061481};
Vmax=49.5 umol/min/mg enzyme toward UDP-glucose (at 70 degrees
Celsius) {ECO:0000269|PubMed:20061481};
pH dependence:
Optimum pH is 7.0 (at 60 degrees Celsius).
{ECO:0000269|PubMed:20061481};
Temperature dependence:
Optimum temperature is 70 degrees Celsius.
{ECO:0000269|PubMed:20061481};
-!- SUBUNIT: Homodimer in solution. {ECO:0000269|PubMed:20061481}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
{ECO:0000305}.
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EMBL; CP000879; ABX31861.1; -; Genomic_DNA.
RefSeq; WP_012208962.1; NC_010003.1.
ProteinModelPortal; A9BHI9; -.
SMR; A9BHI9; -.
STRING; 403833.Pmob_1142; -.
CAZy; GT81; Glycosyltransferase Family 81.
EnsemblBacteria; ABX31861; ABX31861; Pmob_1142.
KEGG; pmo:Pmob_1142; -.
eggNOG; ENOG4105C3Q; Bacteria.
eggNOG; COG0463; LUCA.
HOGENOM; HOG000283250; -.
KO; K13693; -.
OMA; IDPDPMF; -.
OrthoDB; POG091H01A8; -.
BioCyc; MetaCyc:MONOMER-16143; -.
BioCyc; PMOB403833:G1GAG-1177-MONOMER; -.
BRENDA; 2.4.1.266; 11874.
Proteomes; UP000000789; Chromosome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF00535; Glycos_transf_2; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Cobalt; Complete proteome; Glycosyltransferase; Magnesium; Manganese;
Metal-binding; Nickel; Reference proteome; Transferase; Zinc.
CHAIN 1 325 Glucosyl-3-phosphoglycerate synthase.
/FTId=PRO_0000431554.
REGION 37 41 NDP-glucose binding.
{ECO:0000250|UniProtKB:P9WMW9}.
REGION 124 125 NDP-glucose binding.
{ECO:0000250|UniProtKB:P9WMW9}.
REGION 171 174 3-phospho-D-glycerate binding.
{ECO:0000250|UniProtKB:P9WMW9}.
REGION 216 219 NDP-glucose binding.
{ECO:0000250|UniProtKB:P9WMW9}.
REGION 243 248 NDP-glucose binding.
{ECO:0000250|UniProtKB:P9WMW9}.
METAL 126 126 Divalent metal cation.
{ECO:0000250|UniProtKB:P9WMW9}.
METAL 245 245 Divalent metal cation.
{ECO:0000250|UniProtKB:P9WMW9}.
BINDING 71 71 NDP-glucose.
{ECO:0000250|UniProtKB:P9WMW9}.
BINDING 104 104 NDP-glucose.
{ECO:0000250|UniProtKB:P9WMW9}.
BINDING 247 247 3-phospho-D-glycerate.
{ECO:0000250|UniProtKB:P9WMW9}.
BINDING 306 306 NDP-glucose.
{ECO:0000250|UniProtKB:Q73WU1}.
SEQUENCE 325 AA; 37133 MW; 5EF167CEFF7E709C CRC64;
MKDNILKRSF HHSKFENIKE LVKLKEKQDV KISLAFPSLN EEKTIGKEII IMKSELMEKY
PLLDEIAVID SGSEDETVSI AKEYGAKVFY SSDILPEYGF YKGKGENLWK SLYALDGDII
VWVDSDIENI HPKFVYGLVG ALLNYPEIGY VKAFYDRPIV GKSAMQPTGG GRVTELVARP
LFSLFYPELS TIIQPLSGEY AGRREILEKL PFFVGYGVEI AHLIDIAEKF GSEIIAQVDL
ELRIHDNQPL HSLSKMAFEL TKVVLKRLEK YGKLDLNTEL TDKHIMIQKK ENEKVLVPTE
ILSVERPPMI TIPEYKEKFS KEEKV


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